ID   SYV_VIBCH               Reviewed;         953 AA.
AC   Q9KP73;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=VC_2503;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC       inadvertently accommodate and process structurally similar amino acids
CC       such as threonine, to avoid such errors, it has a 'posttransfer'
CC       editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC       dependent manner. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC         tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC         COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated threonine is translocated from the
CC       active site to the editing site. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR   EMBL; AE003852; AAF95645.1; -; Genomic_DNA.
DR   PIR; E82068; E82068.
DR   RefSeq; NP_232132.1; NC_002505.1.
DR   RefSeq; WP_000416450.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KP73; -.
DR   SMR; Q9KP73; -.
DR   STRING; 243277.VC_2503; -.
DR   PRIDE; Q9KP73; -.
DR   DNASU; 2615167; -.
DR   EnsemblBacteria; AAF95645; AAF95645; VC_2503.
DR   GeneID; 57741111; -.
DR   KEGG; vch:VC_2503; -.
DR   PATRIC; fig|243277.26.peg.2384; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   BioCyc; VCHO:VC2503-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033705; Anticodon_Ia_Val.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..953
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106243"
FT   COILED          884..952
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           554..558
FT                   /note="'KMSKS' region"
FT   BINDING         557
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   953 AA;  108171 MW;  D93471A33CF4F69C CRC64;
     MEKTYNPTSI EQDLYKTWEE QGYFKPHGDT SKDAYSIMIP PPNVTGSLHM GHAFQDTIMD
     TLIRCQRMKG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TKHDYGRDAF IDKIWEWKAE
     SGGTITKQLR RLGASVDWDR ERFTMDDGFY KAVQEVFVRL YKDDLIYRGK RLVNWDPKLH
     TAISDLEVEN KETKGHMWHF RYPLADGVKT ADGKDYIVVA TTRPETMLGD TGVAVNPEDP
     RYKDLIGKEI ILPIVGRRIP IVGDEHADME KGTGCVKITP AHDFNDYEVG KRHQLPMINI
     LTFDANIRDA AEVFNSNGEA SNAYGTEIPA KYQGMERFAA RKAIVAEFEE LGLLQEIKDH
     DLTVPYGDRG GVVIEPMLTD QWYVRAGILA KPAVEAVENG DIQFVPKQYE NMYFSWMRDI
     QDWCISRQLW WGHRIPAWYD EQGNVFVGRN EEEVRAENNI AADVALRQDD DVLDTWFSSA
     LWTFGTLGWP EKTPELKVFH PTDVLVTGFD IIFFWVARMI MMTMHFCKDE DGKAQVPFKT
     VYVTGLIRDE NGDKMSKSKG NVLDPIDMID GIDLESLVAK RTGNMMQPQL AAKIEKNTRK
     TFENGIEAYG TDSLRFTLAA MASTGRDINW DMKRLEGYRN FCNKLWNASR YVLMNTEEQD
     CGFAAGAELE YSLADKWIES QFELAAKEFN GHIDNFRLDM AANTLYEFIW NQFCDWYLEL
     TKPVLWKGTE AQQRATRRTL ITVLEKTLRL AHPVIPYITE TIWQSVKPLV DGVEGDTIML
     QALPQYDVAN FNQEALDDIE WVKAFITSIR NLRAEYDINP GKPLEVMLKA ANEQDAARIE
     ANKPVLVSLA KLESIRVLAD GEATPACATA LVGKSELMIP MAGLIDKDAE LDRLAKEIAK
     TQGEIARIEG KLGNEGFVAK APEAVITKER EKLAGYQEAL VKLEQQKATI AAL